Evidence map›Paper›PMID 17699634›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2007

The crystal structure of the third signal-recognition particle GTPase FlhF reveals a homodimer with bound GTP.

Gert Bange, Georg Petzold, Klemens Wild, Richard O Parlitz, Irmgard Sinning

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
1.7field-weighted citation impact, top 18% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

39 citing papers in PubMed, 75 citations in OpenAlex.

  1. mSphere · 2026
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  2. Review
  3. Article
  4. Article
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  8. Article
  9. Structure of the GDP-bound state of the SRP GTPase FlhF.Acta crystallographica. Section F, Structural biology communications · 2024
    Article
  10. MAT Gain of Activity Mutation inACS infectious diseases · 2023
    Article
  11. The Vibrio Polar Flagellum: Structure and Regulation.Advances in experimental medicine and biology · 2023
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 2 countries.

Gert BangeHeidelberg University Biochemistry Center (BZH), INF 328, 69120 Heidelberg, Germany.
Georg Petzold
Klemens Wild
Richard O Parlitz
Irmgard Sinning
University of California, Berkeley · USHeidelberg University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Flagella are well characterized as the organelles of locomotion and allow bacteria to react to environmental changes. The assembly of flagella is a multistep process and relies on a complex type III export machinery located in the cytoplasmic membrane. The FlhF protein is essential for the placement and assembly of polar flagella and has been classified as a signal-recognition particle (SRP)-type GTPase. SRP GTPases appeared early in evolution and form a unique subfamily within the guanine nucleotide binding proteins with only three members: the signal sequence-binding protein SRP54, the SRP receptor FtsY, and FlhF. We report the crystal structures of FlhF from Bacillus subtilis in complex with GTP and GMPPNP. FlhF shares SRP GTPase-specific features such as the presence of an N-terminal alpha-helical domain and the I-box insertion. It forms a symmetric homodimer sequestering a composite active site that contains two head-to-tail arranged nucleotides similar to the heterodimeric SRP-targeting complex. However, significant differences to the GTPases of SRP and the SRP receptor include the formation of a stable homodimer with GTP as well as severe modifications and even the absence of motifs involved in regulation of the other two SRP GTPases. Our results provide insights into SRP GTPases and their roles in two fundamentally different protein-targeting routes that both rely on efficient protein delivery to a secretion channel.

Indexed as

Amino Acid MotifsArginineBacillus subtilisBacterial ProteinsBinding SitesCatalysisCrystallography, X-RayDimerizationGuanosine TriphosphateHydrolysisModels, MolecularMonomeric GTP-Binding ProteinsProtein Structure, QuaternaryProtein Structure, TertiarySequence AlignmentStructural Homology, ProteinArginineBacterial ProteinsflhF protein, BacteriaGuanosine TriphosphateMonomeric GTP-Binding Proteins

Identifiers

PMID17699634
PMCPMC1959431
OpenAlexW2069477720

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.